Structure of PDB 4ejy Chain A Binding Site BS02

Receptor Information
>4ejy Chain A (length=289) Species: 273068 (Caldanaerobacter subterraneus subsp. tengcongensis MB4) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKYNVEEKGTKVIVRGIADFNLKETFESGQCFRWNEEEDGSYTGVAYDRV
VNVKLEGDTLIIDNTNLTDFYDIWFDYFDLGRDYGQIKESLSKDPVLKEA
IKFGQGIRILRQDTWETLVSFIVSQNNRIPQIKKVIENLATSFGNPIEYK
GKIYYTFPKPEELVMYDVETIAKTRCGFRAKYIFDAASKVFSGEINLLKL
HEYSTSEIRDILMTINGVGPKVADCVILYSIGRYDTFPTDVWIKRIVEHL
YLKREGTPVEIQLFAIDKFGDLSGFAQQYLFYYGREMGK
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4ejy Crystal structures of MBOgg1 in complex with two abasic DNA ligands
Resolution2.0 Å
Binding residue
(original residue number in PDB)		N126 Q131 R175 G177 F178 R179
Binding residue
(residue number reindexed from 1)		N126 Q131 R175 G177 F178 R179
Binding affinityPDBbind-CN: Kd=0.86nM
Enzymatic activity
Catalytic site (original residue number in PDB) K221 D240
Catalytic site (residue number reindexed from 1) K221 D240
Enzyme Commision number 4.2.99.18: DNA-(apurinic or apyrimidinic site) lyase.
Gene Ontology
Molecular Function
GO:0003684 damaged DNA binding
GO:0003824 catalytic activity
GO:0008534 oxidized purine nucleobase lesion DNA N-glycosylase activity
GO:0140097 catalytic activity, acting on DNA
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair
GO:0006289 nucleotide-excision repair

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4ejy, PDBe:4ejy, PDBj:4ejy
PDBsum4ejy
PubMed23246782
UniProtQ8R5T9

[Back to BioLiP]